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Results 1 - 10 of 19 > >>
EC Number General Information Commentary Reference
Show all pathways known for 2.7.1.35Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.35evolution PdxK belongs to ribokinase enzyme family in which either cysteine or aspartate act as catalytic residue for its activity. The known catalytic mechanism of ribokinase family and for PdxK is the in line displacement mechanism in which hydroxyl group of the substrate is activated by a catalytic base (aspartate) of the enzyme, to make the nucleophilic attack on the gamma-phosphate group of ATP. The active site residues Leu43, Ser47, Ile52, Arg56, Asn87 and Thr227 present in LdPdxK are replaced with Phe43, Thr47, Try52, Val56, Arg86 and Val231 in mammalian PdxKs -, 759346
Show all pathways known for 2.7.1.35Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.35evolution pyridoxine/pyridoxal kinase (PdxK) belongs to the ribokinase family and is involved in the vitamin B6 salvage pathway by phosphorylating pyridoxal (PL) into an active form. In the human malaria parasite, Plasmodium falciparum, PfPdxK functions to salvage vitamin B6 from both itself and its host 759093
Show all pathways known for 2.7.1.35Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.35malfunction in Drosophila, mutations in the dPdxk gene cause chromosome aberrations (CABs) and increased glucose content in larval hemolymph. The phenotype is rescued by the expression of wild-type human PDXK enzyme, although not by human PDXK mutants D87H, V128I, H246Q, and A243G 760178
Show all pathways known for 2.7.1.35Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.35malfunction root growth of a sos4 mutant is significantly decreased when grown on either 100 mM or 200 mM sucrose as compared to root growth on10 mM sucrose. The sos4 mutant plant accumulates phytoglycogen 723449
Show all pathways known for 2.7.1.35Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.35malfunction the four PDXK human variants, D87H, V128I, H246Q, and A243Gf D87H, V128I, H246Q and A243G proteins show reduced catalytic activity and/or reduced affinity for PLP precursors. Although these variants are rare in population and carried in heterozygous condition, it is suggested that in certain metabolic contexts and diseases in which PLP levels are reduced, the presence of these PDXK variants might threaten genome integrity and increase cancer risk 760178
Show all pathways known for 2.7.1.35Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.35more a FIxxIIxL motif at the C-terminus of the disordered repeat motif (XNXH)m that is implicated in binding the WD40 domain and may provide temporal control of PfPdxK through an interaction with a E3 ligase complex. Molecular docking and modelling, overview. Binding structure of AMP-PNP with PdxK 759093
Show all pathways known for 2.7.1.35Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.35more analysis of the binding structures of substrates and products from PdxK-ligand crystal structures, overview -, 759346
Show all pathways known for 2.7.1.35Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.35more comparison of the structure of apo StPLK with its ligand-bound forms 759183
Show all pathways known for 2.7.1.35Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.35more experimental resurrection of the last common ancestor of the hydroxymethyl pyrimidine kinase group based on comparison of hydroxymethyl pyrimidine and pyridoxal kinases. Probably the last common ancestor was not able to use pyridoxal under physiological conditions. The pyridoxal kinase activity present in the current bifunctional enzymes must have appeared in a convergent event independently of the pyridoxal kinase activity of pdxY and pdxK genes. Substrate pyridoxal is 8-times less preferred than the phosphorylation of hydroxymethyl pyrimidine by the last ancestor 738234
Show all pathways known for 2.7.1.35Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.35more in silico analysis of the human and parasite PdxK structure revealing significant differences in the active site region, LdPdxK homology modeling using pyridoxal kinase from Trypanosoma brucei (PDB ID 3ZS7) as a template, molecular dynamics and molecular docking, overview -, 759342
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